Crystal structure of the 14-subunit RNA polymerase I

@article{FernndezTornero2013CrystalSO,
  title={Crystal structure of the 14-subunit RNA polymerase I},
  author={Carlos Fern{\'a}ndez‐Tornero and Mar{\'i}a Moreno-Morcillo and Umar Jan Rashid and Nicholas M. I. Taylor and Federico M. Ruiz and Tim Gruene and Pierre Legrand and Ulrich Steuerwald and Christoph W. M{\"u}ller},
  journal={Nature},
  year={2013},
  volume={502},
  pages={644-649}
}
Protein biosynthesis depends on the availability of ribosomes, which in turn relies on ribosomal RNA production. In eukaryotes, this process is carried out by RNA polymerase I (Pol I), a 14-subunit enzyme, the activity of which is a major determinant of cell growth. Here we present the crystal structure of Pol I from Saccharomyces cerevisiae at 3.0 Å resolution. The Pol I structure shows a compact core with a wide DNA-binding cleft and a tightly anchored stalk. An extended loop mimics the DNA… 

Structural biology: Pivotal findings for a transcription machine

The basic architecture of Pol I resembles those of Pol II and Pol III, but its DNA-binding cleft adopts a wider conformation than seen in the other RNA polymerases, and other unique features also provide insights into the functional roles of its components.

Structure of RNA polymerase I transcribing ribosomal DNA genes

The structures of active transcribing Pol I from yeast solved by two different cryo-electron microscopy approaches suggest a model for the regulation of transcription elongation in which contracted and expanded polymerase conformations are associated with active and inactive states, respectively.

Structure of the human RNA polymerase I elongation complex

The Pol I structure in the post-cleavage backtracked state shows that the C-terminal zinc ribbon of RPA12 inserts into an open funnel and facilitates “dinucleotide cleavage” on mismatched DNA–RNA hybrid.

The human RNA polymerase I structure reveals an HMG-like docking domain specific to metazoans

Adaptations of the metazoan Pol I transcription system may allow efficient release of positive DNA supercoils accumulating downstream of the transcription bubble, and may allow effective release ofpositive DNA super coils accumulating upstream of thecription bubble.

The human RNA polymerase I structure reveals an HMG-like transcription factor docking domain specific to metazoans

Transcription of the ribosomal RNA precursor by RNA polymerase (Pol) I is a major determinant of cellular growth and dysregulation is observed in many cancer types. Here, we present the purification

The cryo-EM structure of a 12-subunit variant of RNA polymerase I reveals dissociation of the A49-A34.5 heterodimer and rearrangement of subunit A12.2

Cryo-EM structures of yeast Pol I elongation complexes (ECs) bound to the nucleotide analog GMPCPP at 3.2 to 3.4 Å resolution provide additional insight into the functional interplay between the Pol I-specific transcription-like factors A49-A34.5 and A12.2.

The cryo-EM structure of a 12-subunit variant of RNA polymerase I reveals dissociation of the A49-A34.5 heterodimer and rearrangement of subunit A12.2.

Cryo-EM structures of yeast Pol I elongation complexes bound to the nucleotide analog GMPCPP at 3.2 to 3.4 resolution provide additional insight into the functional interplay between the Pol I-specific transcription-like factors A49-A34.5 and A12.2.

Structural rearrangement of TFIIS- and TFIIE/TFIIF-like subunits in RNA polymerase I transcription complexes

Cryo-electron microscopy structures of yeast Pol I elongation complexes (ECs) bound to the nucleotide analog GMPCPP at 3.2 to 3.4 Å resolution are presented that provide additional insight into the functional interplay between the TFIIE/TFIIF-like A49-A34.5 heterodimer and the TFIIS-like subunit A12.2 present in Pol I.

Structural mechanism of ATP-independent transcription initiation by RNA polymerase I

Comparison of the three states in this study with the Pol II system suggests that a ratchet motion of the Core Factor-DNA sub-complex at upstream facilitates promoter melting in an ATP-independent manner, distinct from a DNA translocase actively threading the downstream DNA in thePol II PIC.
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